Chapter 9 Basic structure of proteins: current paradigms, trends, and perspective
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Sheetal Dagar
Abstract
Proteins are essential biomolecules, serving as the building blocks of living organisms and playing vital roles in various biological processes. Amino acids, the fundamental units of proteins, consist of an amino group, a carboxyl group, and a unique side chain (R group). There are around 500 known amino acids, with 20 forming the genetic code. The structure of proteins can be categorized into primary, secondary, tertiary, and quaternary levels. Primary structure represents the linear sequence of amino acids, while the secondary structure involves the folding of segments into alpha helices and beta sheets. Tertiary structure results from long-range interactions between amino acids, and quaternary structure refers to the arrangement of multiple polypeptide chains. Protein motifs and domains are specific arrangements of secondary structures, providing functional and structural characteristics. Techniques such as nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography allow the determination of protein 3D structures. NMR is particularly valuable in native and dynamic environments, while X-ray crystallography requires crystallization. Understanding protein structures aids in drug design, biotechnology, and various research fields, contributing to advancements in science and medicine. However, challenges, such as obtaining crystals and nonphysiological conditions, remain in protein structure determination.
Abstract
Proteins are essential biomolecules, serving as the building blocks of living organisms and playing vital roles in various biological processes. Amino acids, the fundamental units of proteins, consist of an amino group, a carboxyl group, and a unique side chain (R group). There are around 500 known amino acids, with 20 forming the genetic code. The structure of proteins can be categorized into primary, secondary, tertiary, and quaternary levels. Primary structure represents the linear sequence of amino acids, while the secondary structure involves the folding of segments into alpha helices and beta sheets. Tertiary structure results from long-range interactions between amino acids, and quaternary structure refers to the arrangement of multiple polypeptide chains. Protein motifs and domains are specific arrangements of secondary structures, providing functional and structural characteristics. Techniques such as nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography allow the determination of protein 3D structures. NMR is particularly valuable in native and dynamic environments, while X-ray crystallography requires crystallization. Understanding protein structures aids in drug design, biotechnology, and various research fields, contributing to advancements in science and medicine. However, challenges, such as obtaining crystals and nonphysiological conditions, remain in protein structure determination.
Chapters in this book
- Frontmatter I
- Contents V
- Contributors VII
- Chapter 1 Introduction to bioinformatics 1
- Chapter 2 Biological databases and bioinformatics tools 13
- Chapter 3 Fundamentals of bioinformatics 41
- Chapter 4 Tools used in sequence alignment 61
- Chapter 5 Recent advances in the discovery of drug molecules: trends, scope, and relevance 83
- Chapter 6 Computer-aided drug design and drug discovery 103
- Chapter 7 Immunoinformatics: computational keys to immune system secrets 123
- Chapter 8 Phylogenetic analysis 141
- Chapter 9 Basic structure of proteins: current paradigms, trends, and perspective 151
- Index 171
Chapters in this book
- Frontmatter I
- Contents V
- Contributors VII
- Chapter 1 Introduction to bioinformatics 1
- Chapter 2 Biological databases and bioinformatics tools 13
- Chapter 3 Fundamentals of bioinformatics 41
- Chapter 4 Tools used in sequence alignment 61
- Chapter 5 Recent advances in the discovery of drug molecules: trends, scope, and relevance 83
- Chapter 6 Computer-aided drug design and drug discovery 103
- Chapter 7 Immunoinformatics: computational keys to immune system secrets 123
- Chapter 8 Phylogenetic analysis 141
- Chapter 9 Basic structure of proteins: current paradigms, trends, and perspective 151
- Index 171
